Information on EC 5.3.1.8 - Mannose-6-phosphate isomerase

Salmonella enterica subsp. enterica serovar Typhimurium

strain DJ77, gene pmi

-

Sphingobium chungbukense DJ77

strain DJ77, gene pmi

-

-

-

-

2624, 2817, 2828

-

Thermoplasma acidophilum

biunctional phosphoglucose/phosphomannose isomerase EC 5.3.1.9 and 5.3.1.8, resp.

Swissprot

Thermus thermophilus KCCM 40879

Trigonella foenum-graecum

-

-

Vigna angularis

-

693863

-

-

-

malfunction

metabolism

6 entries

physiological function

alpha-D-fructose 6-phosphate

alpha-D-mannose 6-phosphate

Pyrococcus furiosus

-

694521

-

r

beta-D-mannose 6-phosphate

beta-D-fructose 6-phosphate

D-Allose

D-Psicose

D-Fructose 6-phosphate

?

D-fructose 6-phosphate

D-glucose 6-phosphate

D-fructose 6-phosphate

D-mannose 6-phosphate

8 entries

D-glucose 6-phosphate

D-fructose 6-phosphate

D-Lyxose

D-Xylulose

D-Mannose

D-Fructose

D-Mannose 6-phosphate

?

D-Mannose 6-phosphate

D-Fructose 6-phosphate

77 entries

D-Ribose

D-Ribulose

D-ribose 5-phosphate

D-ribulose 5-phosphate

D-talose

D-tagatose

L-allose

L-psicose

L-Lyxose

L-Xylulose

L-Mannose

L-Fructose

L-ribose

L-ribulose

L-ribulose

L-ribose

L-talose

L-tagatose

additional information

?

-

16 entries

D-Fructose 6-phosphate

?

D-fructose 6-phosphate

D-mannose 6-phosphate

Leishmania mexicana

Q9GRS9

first step in the biosynthesis of activated mannose donors required for the biosynthesis of various glycoconjugates

652215

-

652215

r

D-Mannose 6-phosphate

?

D-Mannose 6-phosphate

D-Fructose 6-phosphate

15 entries

additional information

?

-

Ba2+

activates

Ca2+

Co2+

Cu2+

Fe2+

Mg2+

Mn2+

Ni2+

Zinc

Zn2+

additional information

9 entries

1,10-phenanthroline

2,2'-dipyridyl

2,3-Butanedione

-

inactivation

5-deoxy-5-(dihydrogenophosphonomethyl)-D-arabinono-1,4-lactone

5-deoxy-5-malonyl-D-arabinonohydroxamic acid

-

-

5-deoxy-5-phosphonomethyl-D-arabinonate

5-deoxy-5-phosphonomethyl-D-arabinonohydrazide

5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

5-phospho-D-arabinonhydrazide

5-phospho-D-arabinonohydroxamic acid

5-phosphoarabinonate

-

662267

6-deoxy-6-carboxymethyl-D-mannose

6-deoxy-6-dicarboxymethyl-D-mannose

6-deoxy-6-dimethylmalonate-D-mannopyranose

6-deoxy-6-phosphonomethyl-D-mannose

6-phospho-2-deoxygluconate

Cassia coluteoides

-

competitive

6-phosphogluconate

6-Phosphomannonate

Cassia coluteoides

-

competitive

8-hydroxyquinoline

-

2806

ADP-glucose

-

0.5 mM, 77.8% of initial activity

Ag+

-

irreversible inhibition in a two-step process, mannose 6-phosphate protects against inactivation. Mutant enzyme Cys150Ala shows 1000fold less sensitivity than the wild-type enzyme

2818

alpha-D-mannose 6-phosphate

-

poor

2807

arabinose 5-phosphate

Ba2+

about 30% inhibition at 0.5 mM

benzyl 2,3,4-tri-O-benzyl-6-deoxy-6-dimethylmalonate-alpha-D-mannopyranoside

benzyl 2,3,4-tri-O-benzyl-6-O-trifluoromethanesulfonyl-alpha-D-mannose

benzyl 2,3,4-tri-O-benzyl-alpha-D-mannose

Cd2+

cysteine

-

2806

D-mannose 1-phosphate

-

0.5 mM, 81.9% of initial activity

diethyldicarbonate

-

dithiothreitol

6 entries

EDTA

14 entries

erythrose 4-phosphate

10 entries

Fe2+

-

12% residual activity at 0.5 mM

fructose 1-phosphate

-

competitive

2821

Galactose 6-hosphate

-

competitive

-

GDP-D-mannose

-

inhibits mannose 6-phosphate isomerase activity of PMI, feedback regulation of this pathway

GDP-mannose

-

0.5 mM, 46.7% of initial activity

glucosamine 6-phosphate

-

competitive

glucose 1-phosphate

-

competitive

glucose 6-phosphate

-

competitive

Hg2+

HgCl2

-

L-ascorbic acid

Arabidopsis thaliana

-

1 mM, 77% residual activity

693149

mannitol 1-phosphate

N,2,3,4,5-pentahydroxypentanamide

-

p-chloromercuribenzoate

Arabidopsis thaliana

-

0.05 mM, 33% residual activity; 0.05 mM, 39% residual activity

693149

PCMB

-

phosphate

-

competitive

ribose 5-phosphate

-

competitive

S-nitroso-acetyl-penicillamine

-

dose- and time-dependent inactivation

652637

Silver sulfadiazine

sorbitol 6-phosphate

-

competitive

Salmonella enterica subsp. enterica serovar Typhimurium

Y3+

-

Zn2+

additional information

8 entries

Ca2+

-

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Co2+

-

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

diphosphate

-

0.5 mM, 120% of initial activity

Mg2+

-

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Mn2+

-

Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

Ni2+

-

order of activation Mg2+ > Ca2+ > Mn2+ > Co2+ > Ni2+

0.00043 - 0.33

beta-D-mannose 6-phosphate

0.06 - 0.44

D-fructose 6-phosphate

0.72 - 3.5

D-glucose 6-phosphate

433

D-Lyxose

pH 7.5, 40°C, recombinant enzyme

946

D-mannose

pH 7.5, 40°C, recombinant enzyme

0.0413 - 243

D-mannose 6-phosphate

30 entries

110

D-ribose

pH 7.5, 40°C, recombinant enzyme

469

D-talose

pH 7.5, 40°C, recombinant enzyme

312

L-allose

pH 7.5, 40°C, recombinant enzyme

998

L-ribose

pH 7.5, 40°C, recombinant enzyme

136 - 308

L-ribulose

0.17 - 4

mannose 6-phosphate

15 entries

additional information

-

enzyme kinetics with D-lyxose and L-ribose, overview

-

3 - 23

beta-D-mannose 6-phosphate

141

D-fructose 6-phosphate

Thermus thermophilus

Q5SIM4

wild type enzyme, pH 7.0, 80°C

7089

D-Lyxose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

3748

D-mannose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

0.076 - 112100

D-mannose 6-phosphate

23 entries

72

D-ribose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

63970

D-talose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

920

L-allose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

17600

L-ribose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

32670 - 81060

L-ribulose

121 - 162

mannose 6-phosphate

70 - 840

beta-D-mannose 6-phosphate

641

D-fructose 6-phosphate

Thermus thermophilus

Q5SIM4

wild type enzyme, pH 7.0, 80°C

87

16.4

D-Lyxose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

1589

3.5

D-mannose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

216

13 - 6685

D-mannose 6-phosphate

12 entries

0.6

D-ribose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

292

6.8

D-talose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

2017

2.9

L-allose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

10165

17.6

L-ribose

Bacillus subtilis

Q9AGZ4

pH 7.5, 40°C, recombinant enzyme

3127

182 - 579

L-ribulose

0.162

5-deoxy-5-malonyl-D-arabinonohydroxamic acid

-

in 50 mM HEPES buffer, pH 7.1, at 25°C

-

0.0006 - 0.002

5-phospho-D-arabinonhydrazide

0.000041 - 0.0008

5-phospho-D-arabinonohydroxamic acid

0.0105 - 0.115

6-deoxy-6-dicarboxymethyl-D-mannose

0.11 - 58

6-phosphogluconate

0.035 - 0.164

erythrose 4-phosphate

0.0014

erythrose-4-phosphate

-

pH 7.4, 50°C

10

N,2,3,4,5-pentahydroxypentanamide

-

in 50 mM HEPES buffer, pH 7.1, at 25°C

3

5-deoxy-5-phosphonomethyl-D-arabinonate

0.37 - 2.2

5-deoxy-5-phosphonomethyl-D-arabinonohydroxamic acid

0.9 - 4.6

6-deoxy-6-carboxymethyl-D-mannose

0.0181 - 0.199

6-deoxy-6-dicarboxymethyl-D-mannose

1.61 - 4.7

6-deoxy-6-phosphonomethyl-D-mannose

0.01

wild type enzyme, using ribose 5-phosphate as substrate, at pH 7.0 and 80°C

0.0101

recombinant enzyme

0.0165

recombinant enzyme

0.0225

recombinant enzyme

0.0659

recombinant enzyme

0.0918

recombinant enzyme

0.269

-

enzyme activity in cells after 54 h growth on maltose

701879

0.3

mutant enzyme E132D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme W13A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

0.306

Alcaligenes sp.

-

enzyme activity in cells after 54 h growth on sucrose

701879

0.313

Alcaligenes sp.

-

enzyme activity in cells after 54 h growth on glucose

701879

0.6

mutant enzyme E67Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

0.74

wild type enzyme, using ribulose 5-phosphate as substrate, at pH 7.0 and 80°C

1.4

mutant enzyme E132A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.5

mutant enzyme H122Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme H50Q, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Q48A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.7

mutant enzyme H50A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

1.9

mutant enzyme E67A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme R142A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

2.1

mutant enzyme H122A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

2.8

mutant enzyme E67D, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

3 - 8

mutant enzyme W69A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

3

-

wild type enzyme, using D-psicose as substrate, at pH 7.0 and 75°C

4.5

wild type enzyme, using D-fructose 6-phosphate as substrate, at pH 7.0 and 80°C

5.95

-

11

mutant enzyme K65A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

16

19

-

wild type enzyme, using L-mannose as substrate, at pH 7.0 and 75°C

22

-

wild type enzyme, using L-xylulose as substrate, at pH 7.0 and 75°C

23

-

wild type enzyme, using L-lyxose as substrate, at pH 7.0 and 75°C

31

mutant enzyme W13F, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

33.5

-

39

mutant enzyme W13H, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C; mutant enzyme Y124A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

40

mutant enzyme L39A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

42

-

wild type enzyme, using L-psicose as substrate, at pH 7.0 and 75°C

44

mutant enzyme D138A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

51

mutant enzyme W13Y, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

57

-

wild type enzyme, using L-fructose as substrate, at pH 7.0 and 75°C

58

63

-

wild type enzyme, using L-talose as substrate, at pH 7.0 and 75°C

75

80

-

85

-

wild type enzyme, using D-tagatose as substrate, at pH 7.0 and 75°C

126

-

wild type enzyme, using D-ribulose as substrate, at pH 7.0 and 75°C

128

-

wild type enzyme, using D-xylulose as substrate, at pH 7.0 and 75°C

165

-

wild type enzyme, using D-allose as substrate, at pH 7.0 and 75°C

167

-

wild type enzyme, using D-fructose as substrate, at pH 7.0 and 75°C

194

mutant enzyme R11A, using D-mannose 6-phosphate as substrate, at pH 7.0 and 80°C

333

-

wild type enzyme, using D-lyxose as substrate, at pH 7.0 and 75°C

380

-

2828

420

-

2828

425

-

wild type enzyme, using L-ribose as substrate, at pH 7.0 and 75°C

474

-

mutant enzyme K37A, using L-ribulose as substrate, at pH 7.0 and 75°C

742

-

wild type enzyme, using L-allose as substrate, at pH 7.0 and 75°C

838

-

mutant enzyme W13A, using L-ribulose as substrate, at pH 7.0 and 75°C

842

-

wild type enzyme, using D-mannose as substrate, at pH 7.0 and 75°C

890

-

purified recombinant enzyme

972

-

mutant enzyme D138A, using L-ribulose as substrate, at pH 7.0 and 75°C

1011

-

mutant enzyme K65A, using L-ribulose as substrate, at pH 7.0 and 75°C

1016

-

mutant enzyme Q48A, using L-ribulose as substrate, at pH 7.0 and 75°C

1045

-

mutant enzyme R142E, using L-ribulose as substrate, at pH 7.0 and 75°C

1046

-

mutant enzyme W69A, using L-ribulose as substrate, at pH 7.0 and 75°C

1065

-

mutant enzyme L39A, using L-ribulose as substrate, at pH 7.0 and 75°C

1076

-

mutant enzyme L124A, using L-ribulose as substrate, at pH 7.0 and 75°C

1092

-

mutant enzyme R142Y, using L-ribulose as substrate, at pH 7.0 and 75°C

1194

-

mutant enzyme L18A, using L-ribulose as substrate, at pH 7.0 and 75°C

1214

-

mutant enzyme R142K, using L-ribulose as substrate, at pH 7.0 and 75°C

1270

-

mutant enzyme R142Q, using L-ribulose as substrate, at pH 7.0 and 75°C

1482

-

mutant enzyme R11A, using L-ribulose as substrate, at pH 7.0 and 75°C

1493

-

wild type enzyme, using L-ribulose as substrate, at pH 7.0 and 75°C

1619

-

wild type enzyme, using D-talose as substrate, at pH 7.0 and 75°C

1791

-

mutant enzyme R142A, using L-ribulose as substrate, at pH 7.0 and 75°C

2152

-

mutant enzyme R14N, using L-ribulose as substrate, at pH 7.0 and 75°C

additional information

6.5 - 7

-

6.5 - 8

7

7 - 7.2

-

7

7.1

7.4

-

7.5

7.6

8

-

Salmonella enterica subsp. enterica serovar Typhimurium

8.5

-

5.5 - 9

-

about 50% of maximal activity at pH 5.5 and pH 9.0

6 - 11

Cassia coluteoides

-

pH 6.0: 50% of maximal activity, relative high activity up to pH 11

6.3 - 8.8

-

more than 50% of maximum activity in this range

6.5 - 8.5

Salmonella enterica subsp. enterica serovar Typhimurium

6.5 - 9

activity range

6.5 - 8.5

-

22

Salmonella enterica subsp. enterica serovar Typhimurium

assay at room temperature

25

37

40

recombinant enzyme

52

-

70

75

-

maximal activity of the recombinant enzyme for L-ribulose isomerization

80

-

95

Pyrococcus horikoshii

O58649

-

733811

100

-

20 - 50

-

60 - 80

-

70 - 90

-

5.9

-

calculated

6

calculated

-

-

cell suspension culture

Vigna angularis

-

growth on liquid and solid media, but no in presence of 90 mM mannose. After transfer of sucrose-grown cell onto medium containing mannose, cells grew little initially, but after a month lag period, they start to form callus colonies. Mannose-accomodated cells are capable of converting mannose to sucrose, with enhanced phosphomannose isomerase activity

693863

corm

-

digestive gland

Placopecten magellanicus

-

Placopecten magellanicus

-

-

-

-

-

pod

-

Cassia coluteoides

-

developing and germinating

-

-

additional information

2gz6, download, 3D-view

1qwr, download, 3D-view

SCOPe (1qwr)

CATH (1qwr)

Bacillus subtilis (strain 168)

P39841

1pmi, download, 3D-view

SCOPe (1pmi)

CATH (1pmi)

Candida albicans (strain SC5314 / ATCC MYA-2876)

P34948

1tzb, download, 3D-view

SCOPe (1tzb)

CATH (1tzb)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1tzc, download, 3D-view

SCOPe (1tzc)

CATH (1tzc)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1x9h, download, 3D-view

SCOPe (1x9h)

CATH (1x9h)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

1x9i, download, 3D-view

SCOPe (1x9i)

CATH (1x9i)

Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)

2wfp, download, 3D-view

SCOPe (2wfp)

CATH (2wfp)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1m, download, 3D-view

SCOPe (3h1m)

CATH (3h1m)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1w, download, 3D-view

SCOPe (3h1w)

CATH (3h1w)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

3h1y, download, 3D-view

SCOPe (3h1y)

CATH (3h1y)

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

29000

-

gel filtration

29100

gel filtration

36000

-

gel filtration, recombinant enzyme

36600

gel filtration, recombinant enzyme

45000

46520

-

calculation from nucleotide sequence encoded by cDNA

2826

46530

-

recombinant enzyme, electrospray mass spectroscopy

2826

48000

Thermoplasma acidophilum

Q9HIC2

gel filtration

662220

48740

-

wild-type recombinant enzyme, electrospray mass spectroscopy

49060

-

selenomethionine-labelled enzyme expressed in E. coli, electrospray mass spectroscopy

53000

Pyrococcus furiosus

-

SDS-PAGE

694521

54000

58000

-

gel filtration

59000

Glycine max

-

gel filtration

Trigonella foenum-graecum

63000

-

gel filtration

65000

-

sedimentation equilibrium, analytical ultracentrifugation

67000

68000

Cassia coluteoides

-

enzyme from pods, gel filtration

74500

Cassia coluteoides

-

enzyme from pods and seeds, density gradient centrifugation

?

dimer

monomer

additional information

-

-

2820, 2822, 2825

homology modeling of structure and refinement by energy minimization and molecular dynamics

-

681498

-

-

660585

both in complex with fructose 6-phosphate and with glucose 6-phosphate

661100

both native form and in complex with 5-phosphoarabinonate

Salmonella enterica subsp. enterica serovar Typhimurium

662267

enzyme in apoform without metal ion, in the holoform with bound Zn2+, or complexed with bound inhibitor yttrium, or with Zn2+ and fructose 6-phosphate, microbatch method, 0.003 ml of protein solution and crystallization solution are mixed containing 4 mg/ml protein, 0.1 M magnesium acetate, 0.2 M sodium cacodylate, pH 6.5, 20% PEG 8000 and 5% dioxane, addition of 10 mM metal ions and 250 mM fructose 6-phosphate for complexed enzyme, X-ray diffraction structure determination and analysis at 1.7-2.5 A resolution, molecular replacement

Salmonella enterica subsp. enterica serovar Typhimurium

to 1.66 A resolution, space group P212121. Preliminary structure solution by molecular replacement using the strucutre from Candida albicans mannose-6-phosphate isomerase

-

690273

5.5

-

40°C, 1 h, about 35% loss of activity

2810

6 - 9.5

-

40°C, 1 h, no loss of activity

2810

6.5 - 8

-

4°C, stable

2827

10

-

40°C, 1 h, about 25% loss of activity

2810

25

purified recombinant enzyme, half-life is 461 h

28

-

half-life in absence of Zn2+: 110 min, half-life in presence of 0.0002 mM ZnCl2: 270 min

30

purified recombinant enzyme, half-life is 325 h

35

purified recombinant enzyme, half-life is 236 h

37

-

6 min, wild-type enzyme stable, mutant enzyme loses about 90% of activity

40

45

50

purified recombinant enzyme, half-life is 10 h

55

-

pH 6.5, 10 min, about 75% loss of native enzyme

60

-

enzyme half-life is 388 h

64 - 85

the half-lives of the enzyme at 65, 70, 75, 80, and 85°C are 13, 6.5, 3.7, 1.8, and 0.2 h, respectively

65

-

enzyme half-life is 73 h

65 - 85

-

the enzyme shows half-lives of 22, 10, 5.5, 2.1, and 0.3 h at 65, 70, 75, 80, and 85°C, respectively

70

-

enzyme half-life is 27 h

100

-

melting temperature for thermal unfolding, 60 min, 50% residual activity

additional information

EDTA-treated enzyme and 1,10-phenanthroline-treated enzyme is more susceptible to heat denaturation, addition of various metal ions causes the recovery of thermal stability. The most effective metal ion is Co2+, which causes the recovery of thermal stability to a level higher than that of the native enzyme

-

-20°C, unstable

-

-

HisTrap HP column chromatography

HiTrap Ni-chelating column chromatography and Q-Sepharose column chromatography

-

Ni-affinity column

-

normal and selenomethionine-labelled enzyme expressed in Escherichia coli

-

recombinant enzyme 27fold from Escherichia coli strain ER2566 by affinity chromatography

recombinant enzyme 8.7fold from Escherichia coli strain ER2566

-

recombinant His6-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography

-

Salmonella enterica subsp. enterica serovar Typhimurium

recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography

-

6 entries

Agrobacterium-based expression in Linum usitatissimum

-

682360

cDNA under the control of the GAL1 promoter, expression in Saccharomyces cerevisiae and in Escherichia coli

-

2826

expressed in Escherichia coli BL21 Codon Plus (DE3)-RIPL strain

Pyrococcus furiosus

-

694521

expressed in Escherichia coli ER2566 cells

expressed in Escherichia coli GI724 cells

Brassica rapa subsp. chinensis

-

716883

expressed in Nicotiana tabacum transformed with Agrobacterium tumefaciens

G1E7A7

728283

expressed in Oryza sativa ssp. japonica varieties Wanjing97 and Nipponbare

-

728469

expression in Agrobacterium tumefaciens

Arabidopsis thaliana

Q9M884

700488

expression in Brassica rapa

-

681607, 682359

expression in Escherichia coli

expression in Escherichia coli strain ER2566

expression in Escherichia coli strain ER2566, coexpression with L-arabinose isomerase

-

701812

expression in Pseudomonas aeruginosa

-

3354

gene pmi, DNA and amino acid sequence determination and analysis, expression of the His6-tagged enzyme in Escherichia coli strain BL21 (DE3)

-

high level expression in Escherichia coli M15 as inclusion bodies

Leishmania mexicana

Q9GRS9

652215

overexpressed under the control of the tac promoter in the broad-host-range controlled-expression vector pMMB22, expression in Escherichia coli

-

2814

overexpression in both mucoid and nonmucoid strains of Pseudomonas aeruginosa

Salmonella enterica subsp. enterica serovar Typhimurium

-

3354

overexpression of the N-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)

use of enzyme as selectable marker

-

682353

wild-type and selenomethionine-labelled enzyme expressed in Escherichia coli

-

C150A

-

mutant Cys150Ala shows similar Km-values and maximal velocity as compared to the wild-type enzyme. The mutant enzyme shows no inhibition by silver sulfadiazine, and is 1000fold less sensitive to Hg2+ inhibition

2818

L129F

the activity of the mutant is 204% of the activity of the wild type enzyme

L129W

the activity of the mutant is 10% of the activity of the wild type enzyme

L129Y

the activity of the mutant is 94% of the activity of the wild type enzyme

N90A/L129F

the activity of the mutant is about 6fold higher than the activity of the wild type enzyme

W17Q/N90A/L129F

the specific activity and catalytic efficiency for L-ribulose isomerization of this variant are 3.1 and 7.1fold higher, respectively, than those of the wild type enzyme at pH 7.0 and 70°C in the presence of 1mM Co2+

E410A

-

about 25% of wild-type catalytic efficiency

E458A

-

about 25% of wild-type catalytic efficiency

H411A

-

about 25% of wild-type catalytic efficiency

N433A

-

about 25% of wild-type catalytic efficiency

R373A

-

about 4% of wild-type catalytic efficiency

R408A

-

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R408K

-

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

R472A

-

about 1% of wild-type catalytic efficiency

R479A

-

about 3% of wild-type catalytic efficiency

E410A

-

about 25% of wild-type catalytic efficiency

-

H411A

-

about 25% of wild-type catalytic efficiency

-

R408A

-

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

-

R408K

-

complete loss of phosphomannose isomerase activity without affecting guanosine diphosphate-D-mannose diphosphorylase activity

-

R479A

-

about 3% of wild-type catalytic efficiency

-

D138A

E132A

E132D

the mutant shows 0.4% activity compared to the wild type enzyme

E132K

inactive

E132Q

inactive

E132W

inactive

E67A

E67D

the mutant shows 3.7% activity compared to the wild type enzyme

E67K

inactive

E67Q

the mutant shows 0.8% activity compared to the wild type enzyme

E67W

inactive

H122A

H122D

inactive

H122K

inactive

H122Q

the mutant shows 2.0% activity compared to the wild type enzyme

H122W

inactive

H50A

H50D

inactive

H50K

inactive

H50Q

the mutant shows 2.0% activity compared to the wild type enzyme

H50W

inactive

K37A

K65A

L124A

-

the enzyme shows decreased specific activity for L-ribulose

L18A

L39A

Q48A

Q48D

inactive

Q48K

inactive

Q48N

inactive

Q48W

inactive

R11A

R142A

R142D

inactive

R142E

-

the enzyme shows decreased specific activity for L-ribulose

R142K

R142N

R142Q

-

the enzyme shows decreased specific activity for L-ribulose

R142W

inactive

R142Y

-

the enzyme shows decreased specific activity for L-ribulose

W13A

W13D

inactive

W13F

the mutant shows 41% activity compared to the wild type enzyme

W13H

the mutant shows 52% activity compared to the wild type enzyme

W13K

inactive

W13Q

inactive

W13Y

the mutant shows 68% activity compared to the wild type enzyme

W69A

Y124A

the mutant shows 52% activity compared to the wild type enzyme

E132A

Thermus thermophilus KCCM 40879

-

the mutants has no activity for L-ribulose; the mutant shows 1.9% activity compared to the wild type enzyme

-

E132D

Thermus thermophilus KCCM 40879

-

the mutant shows 0.4% activity compared to the wild type enzyme

-

E132Q

Thermus thermophilus KCCM 40879

-

inactive

-

H122A

Thermus thermophilus KCCM 40879

-

the mutants has no activity for L-ribulose; the mutant shows 2.8% activity compared to the wild type enzyme

-

K37A

Thermus thermophilus KCCM 40879

-

the enzyme shows decreased specific activity for L-ribulose; the mutant shows 21% activity compared to the wild type enzyme

-

R11A

Thermus thermophilus KCCM 40879

-

the enzyme shows about wild type specific activity for L-ribulose

-

R142K

Thermus thermophilus KCCM 40879

-

the enzyme shows decreased specific activity for L-ribulose

-

additional information

13 entries

agriculture